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Crystallization and preliminary crystallographic analysis of latent, active and recombinantly expressed aurone synthase, a polyphenol oxidase, from

DOI: 10.1107/S2053230X15007542 DOI Help
PMID: 26057806 PMID Help

Authors: Christian Molitor (Institut für Biophysikalische Chemie, Fakultät für Chemie, Universität Wien) , Stephan Mauracher (University of Vienna) , Annette Rompel (Universitat Wien)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Acta Crystallographica Section F Structural Biology Communications , VOL 71 , PAGES 746 - 751

State: Published (Approved)
Published: June 2015
Diamond Proposal Number(s): 8476

Open Access Open Access

Abstract: Aurone synthase (AUS), a member of a novel group of plant polyphenol oxidases (PPOs), catalyzes the oxidative conversion of chalcones to aurones. Two active cgAUS1 (41.6 kDa) forms that differed in the level of phosphorylation or sulfation as well as the latent precursor form (58.9 kDa) were purified from the petals of Coreopsis grandiflora. The differing active cgAUS1 forms and the latent cgAUS1 as well as recombinantly expressed latent cgAUS1 were crystallized, resulting in six different crystal forms. The active forms crystallized in space groups P212121 and P1211 and diffracted to ∼1.65 Å resolution. Co-crystallization of active cgAUS1 with 1,4-resorcinol led to crystals belonging to space group P3121. The crystals of latent cgAUS1 belonged to space group P1211 and diffracted to 2.50 Å resolution. Co-crystallization of recombinantly expressed pro-AUS with the hexatungstotellurate(VI) salt Na6[TeW6O24] within the liquid–liquid phase separation zone significantly improved the quality of the crystals compared with crystals obtained without hexatungstotellurate(VI).

Journal Keywords: Aurone synthase; latent proenzyme; polyphenol oxidase; liquid–liquid phase separation; polyoxometalate.

Subject Areas: Biology and Bio-materials

Instruments: I04-1-Macromolecular Crystallography (fixed wavelength)

Other Facilities: ESRF; DESY

Added On: 12/01/2016 12:52

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